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Q8K0C4

- CP51A_MOUSE

UniProt

Q8K0C4 - CP51A_MOUSE

Protein

Lanosterol 14-alpha demethylase

Gene

Cyp51a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.By similarity

    Catalytic activityi

    A 14-alpha-methylsteroid + 3 O2 + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP+ + 4 H2O.

    Cofactori

    Heme group.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi449 – 4491Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. heme binding Source: UniProtKB
    2. iron ion binding Source: InterPro
    3. sterol 14-demethylase activity Source: UniProtKB

    GO - Biological processi

    1. cholesterol biosynthetic process Source: MGI
    2. cholesterol biosynthetic process via 24,25-dihydrolanosterol Source: Ensembl
    3. demethylation Source: GOC
    4. steroid biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    ReactomeiREACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_208531. Cholesterol biosynthesis.
    REACT_227038. Endogenous sterols.
    UniPathwayiUPA00770; UER00754.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lanosterol 14-alpha demethylase (EC:1.14.13.70)
    Short name:
    LDM
    Alternative name(s):
    CYPLI
    Cytochrome P450 51A1
    Cytochrome P450-14DM
    Short name:
    Cytochrome P45014DM
    Cytochrome P450LI
    Sterol 14-alpha demethylase
    Gene namesi
    Name:Cyp51a1
    Synonyms:Cyp51
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:106040. Cyp51.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 503503Lanosterol 14-alpha demethylasePRO_0000376796Add
    BLAST

    Proteomic databases

    MaxQBiQ8K0C4.
    PaxDbiQ8K0C4.
    PRIDEiQ8K0C4.

    PTM databases

    PhosphoSiteiQ8K0C4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8K0C4.
    BgeeiQ8K0C4.
    GenevestigatoriQ8K0C4.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1853747.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K0C4.
    SMRiQ8K0C4. Positions 14-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei24 – 4421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2124.
    GeneTreeiENSGT00660000095370.
    HOGENOMiHOG000042780.
    InParanoidiQ9JIP8.
    KOiK05917.
    OMAiMIHTPHN.
    OrthoDBiEOG7PZRX3.
    PhylomeDBiQ8K0C4.
    TreeFamiTF105091.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00465. EP450IV.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8K0C4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLLGLLQSG GWVLGQAMEQ VTGGNLLSTL LIACAFTLSL VYLFRLAVGH    50
    MVQLPAGAKS PPHIYSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM 100
    VGKTFTYLLG SDAAALLFNS KNEDLNAEEV YGRLTTPVFG KGVAYDVPNA 150
    IFLEQKKIIK SGLNIAHFKQ YVPIIEKEAK EYFQSWGESG ERNVFEALSE 200
    LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFTHAAWL LPAWLPLPSF 250
    RRRDRAHREI KNIFYKAIQK RRLSKEPAED ILQTLLDSTY KDGRPLTDEE 300
    ISGMLIGLLL AGQHTSSTTS AWMGFFLAKD KPLQEKCYLE QKAVCGEDLP 350
    PLTYDQLKDL NLLDRCIKET LRLRPPIMTM MRMAKTPQTV AGYTIPPGHQ 400
    VCVSPTVNQR LKDSWAERLD FNPDRYLQDN PASGEKFAYV PFGAGRHRCV 450
    GENFAYVQIK TIWSTMLRLY EFDLINGYFP TVNYTTMIHT PENPVIRYKR 500
    RSK 503
    Length:503
    Mass (Da):56,776
    Last modified:October 1, 2002 - v1
    Checksum:i6A4BBA350F1D85C7
    GO

    Sequence cautioni

    The sequence AAF73986.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191E → A in AAF74562. (PubMed:10864439)Curated
    Sequence conflicti98 – 981F → L in AAF74562. (PubMed:10864439)Curated
    Sequence conflicti98 – 981F → L in AAF73986. (PubMed:10653123)Curated
    Sequence conflicti235 – 2351T → A in BAC27231. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF204804
    , AF204796, AF204797, AF204798, AF204799, AF204800, AF204801, AF204802, AF204803 Genomic DNA. Translation: AAF74562.1.
    AF166266 mRNA. Translation: AAF73986.1. Different initiation.
    AK028355 mRNA. Translation: BAC25900.1.
    AK028815 mRNA. Translation: BAC26134.1.
    AK031059 mRNA. Translation: BAC27231.1.
    AK076983 mRNA. Translation: BAC36548.1.
    CH466600 Genomic DNA. Translation: EDL14627.1.
    BC031813 mRNA. Translation: AAH31813.1.
    CCDSiCCDS19071.1.
    RefSeqiNP_064394.2. NM_020010.2.
    UniGeneiMm.140158.

    Genome annotation databases

    EnsembliENSMUST00000001507; ENSMUSP00000001507; ENSMUSG00000001467.
    GeneIDi13121.
    KEGGimmu:13121.
    UCSCiuc008wie.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF204804
    , AF204796 , AF204797 , AF204798 , AF204799 , AF204800 , AF204801 , AF204802 , AF204803 Genomic DNA. Translation: AAF74562.1 .
    AF166266 mRNA. Translation: AAF73986.1 . Different initiation.
    AK028355 mRNA. Translation: BAC25900.1 .
    AK028815 mRNA. Translation: BAC26134.1 .
    AK031059 mRNA. Translation: BAC27231.1 .
    AK076983 mRNA. Translation: BAC36548.1 .
    CH466600 Genomic DNA. Translation: EDL14627.1 .
    BC031813 mRNA. Translation: AAH31813.1 .
    CCDSi CCDS19071.1.
    RefSeqi NP_064394.2. NM_020010.2.
    UniGenei Mm.140158.

    3D structure databases

    ProteinModelPortali Q8K0C4.
    SMRi Q8K0C4. Positions 14-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1853747.

    PTM databases

    PhosphoSitei Q8K0C4.

    Proteomic databases

    MaxQBi Q8K0C4.
    PaxDbi Q8K0C4.
    PRIDEi Q8K0C4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001507 ; ENSMUSP00000001507 ; ENSMUSG00000001467 .
    GeneIDi 13121.
    KEGGi mmu:13121.
    UCSCi uc008wie.1. mouse.

    Organism-specific databases

    CTDi 13121.
    MGIi MGI:106040. Cyp51.

    Phylogenomic databases

    eggNOGi COG2124.
    GeneTreei ENSGT00660000095370.
    HOGENOMi HOG000042780.
    InParanoidi Q9JIP8.
    KOi K05917.
    OMAi MIHTPHN.
    OrthoDBi EOG7PZRX3.
    PhylomeDBi Q8K0C4.
    TreeFami TF105091.

    Enzyme and pathway databases

    UniPathwayi UPA00770 ; UER00754 .
    Reactomei REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_208531. Cholesterol biosynthesis.
    REACT_227038. Endogenous sterols.

    Miscellaneous databases

    NextBioi 283158.
    PROi Q8K0C4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8K0C4.
    Bgeei Q8K0C4.
    Genevestigatori Q8K0C4.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00465. EP450IV.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the mouse lanosterol 14alpha-demethylase (CYP51), a new member of the evolutionarily most conserved cytochrome P450 family."
      Debeljak N., Horvat S., Vouk K., Lee M., Rozman D.
      Arch. Biochem. Biophys. 379:37-45(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    2. "Molecular cloning and partial characterisation of the mouse Cyp51 cDNA."
      Debeljak N., Horvat S., Komel R., Rozman D.
      Pflugers Arch. 439:R7-R8(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: 129/Sv.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo, Placenta, Skin and Testis.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Salivary gland.

    Entry informationi

    Entry nameiCP51A_MOUSE
    AccessioniPrimary (citable) accession number: Q8K0C4
    Secondary accession number(s): Q8BSQ7, Q9JIP8, Q9JIY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2009
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3